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| Catalog # | Availability | Size | Quantity | Unit Price | Save For Later Wish List | |
|---|---|---|---|---|---|---|
| VAG0436-2 | 7 days | 2 µg | $120.00 |
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| VAG0436-10 | 7 days | 10 µg | $290.00 | |||
| VAG0436-100 | 7 days | 100 µg | $1,760.00 |
Product Overview | |
| Name | SARS MERS RBD, Active |
|---|---|
| Description | |
| SARS MERS Spike Receptor Binding Domain Recombinant, Active | |
| Accession (Primary) | K0BRG7 |
| Synonyms | |
| Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERSCoV S2 P, Spike2 glycoprotein, S2 glycoprotein, S2, Spike S2 Subunit protein, S2 Subunit | |
| Introduction | |
| Since April 2012, cases of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV) have been identified in various countries. Coronaviruses are the cause of the common cold, SARS (severe acute respiratory syndrome) and other severe illnesses with high mortality rates, all are classified into coronavirus family. MERS-CoV is a new type of SARS found in the coronavirus family causing severe pneumonia with sudden and serious respiratory illness with high mortality rates as well. Since January 27 th 2015, the WHO has reported 956 human cases, including 351 deaths. More cases of the new coronavirus strain are expected. Like in other coronaviruses, large surface spike glycoprotein is a central structural protein of this virus; it is located above the virion surface to bind and enter into the target cell. Spike protein has 2 domains- S1 and S2. The S1 domain is responsible for cellular tropism and interaction with target cell, while the S2 domain is responsible for membrane fusion. The C-terminal of S1 domain contains a receptor binding domain, and is also a potential target for vaccine development and an antigen for diagnosis. | |
| Source | |
| Sf9, Baculovirus cells. | |
| Physical Appearance | |
| Sterile filtered colorless solution. | |
| Formulation | |
| The SARS MERS S2 solution (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4). | |
| Stability | |
| Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles. | |
| Purity | |
| Greater than 85.0% as determined by SDS-PAGE. | |
| Amino acid sequence | |
| ADP SVPGEMR LASIAFNHPI QVDQLNSSYF KLSIPTNFSF GVTQEYIQTT IQKVTVDCKQ YVCNGFQKCE QLLREYGQFC SKINQALHGA NLRQDDSVRN LFASVKSSQS SPIIPGFGGD FNLTLLEPVS ISTGSRSARS AIEDLLFDKV TIADPGYMQG YDDCMQQGPA SARDLICAQY VAGYKVLPPL MDVNMEAAYT SSLLGSIAGV GWTAGLSSFA AIPFAQSIFY RLNGVGITQQ VLSENQKLIA NKFNQALGAM QTGFTTTNEA FQKVQDAVNN NAQALSKLAS ELSNTFGAIS ASIGDIIQRL DVLEQDAQID RLINGRLTTL NAFVAQQLVR SESAALSAQL AKDKVNECVK AQSKRSGFCG QGTHIVSFVV NAPNGLYFMH VGYYPSNHIE VVSAYGLCDA ANPTNCIAPV NGYFIKTNNT RIVDEWSYTG SSFYAPEPIT SLNTKYVAPQ VTYQNISTNL PPPLLGNSTG IDFQDELDEF FKNVSTSIPN FGSLTQINTT LLDLTYEMLS LQQVVKALNE SYIDLKELGN YTYYNKWP HH HHHH | |
| Precautions | |
| SARS MERS RBD, Active is for research use only and not for use in diagnostic or therapeutic procedures. | |
Target Information: ( K0BRG7 ) | |
Background |
The severe acute respiratory syndrome coronavirus (SARS-CoV) and Middle East respiratory syndrome coronavirus (MERS-CoV) have posed significant global health threats in recent years. Central to their pathogenesis is the interaction between the viral spike proteins and host cell receptors. This research aims to investigate the receptor binding domain (RBD) of SARS and MERS spike proteins and its implications for viral entry and the development of therapeutic interventions. Understanding the molecular mechanisms underlying viral-host interactions can pave the way for targeted therapeutic strategies against these deadly coronaviruses. Structure and Function of SARS and MERS Spike RBD: The spike proteins of SARS-CoV and MERS-CoV are critical for viral entry into host cells. These proteins consist of two subunits: S1, responsible for receptor binding, and S2, involved in membrane fusion. The receptor binding domain (RBD) within the S1 subunit specifically interacts with host cell receptors, enabling viral attachment and entry. The RBDs of SARS and MERS spike proteins exhibit unique structural features and binding affinities for their respective receptors. Interaction with ACE2 and DPP4 Receptors: The SARS-CoV spike protein RBD interacts with the angiotensin-converting enzyme 2 (ACE2) receptor, which is abundantly expressed in the respiratory tract. The binding of SARS-CoV RBD to ACE2 facilitates viral entry into host cells. On the other hand, the MERS-CoV spike protein RBD interacts with the dipeptidyl peptidase 4 (DPP4) receptor, predominantly expressed in the lungs and other tissues. The ACE2 and DPP4 receptors play crucial roles in determining the host range and tissue tropism of SARS and MERS coronaviruses. Implications for Viral Pathogenesis: The binding of SARS and MERS spike RBDs to their respective receptors triggers conformational changes in the spike protein, leading to membrane fusion and subsequent viral entry. This process is crucial for viral replication and the spread of infection within the host. The specificity and affinity of the RBD-receptor interaction influence viral tropism, tissue damage, and disease severity. Understanding the determinants of RBD-receptor binding can provide insights into viral pathogenesis and potential therapeutic targets. Development of Therapeutic Interventions: The RBD of SARS and MERS spike proteins represents a promising target for the development of antiviral therapeutics. Several strategies have been explored, including monoclonal antibodies and small molecule inhibitors, to disrupt the RBD-receptor interaction and inhibit viral entry. These approaches aim to block the binding interface between the spike RBD and the host receptor, thereby preventing viral attachment and entry. Additionally, vaccine development efforts have focused on generating neutralizing antibodies against the RBD to elicit protective immune responses. Conclusion: The investigation of the receptor binding domain (RBD) of SARS and MERS spike proteins sheds light on the molecular mechanisms underlying viral entry and pathogenesis. The specific interactions between the spike RBD and host cell receptors play a crucial role in determining viral tropism and tissue damage. Targeting the RBD-receptor interaction holds promise for the development of effective therapeutics against SARS-CoV, MERS-CoV, and potentially other related coronaviruses. Further research and development efforts are needed to exploit the potential of the spike RBD as a therapeutic target and to combat future coronavirus outbreaks. |
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